TEV1_BPT4
ID TEV1_BPT4 Reviewed; 245 AA.
AC P13299; Q9T0T3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Intron-associated endonuclease 1;
DE EC=3.1.-.-;
DE AltName: Full=I-TevI;
DE AltName: Full=IRF protein;
GN Name=ITEVIR;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ALC4;
RX PubMed=3698096; DOI=10.1016/0092-8674(86)90379-x;
RA Chu F.K., Maley G.F., West D.K., Belfort M., Maley F.;
RT "Characterization of the intron in the phage T4 thymidylate synthase gene
RT and evidence for its self-excision from the primary transcript.";
RL Cell 45:157-166(1986).
RN [2]
RP SEQUENCE REVISION TO 67.
RA Chu F.K.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP IDENTIFICATION OF PROTEIN.
RX PubMed=2543665; DOI=10.1016/s0021-9258(18)81624-6;
RA West D.K., Changchien L.-M., Maley G.F., Maley F.;
RT "Evidence that the intron open reading frame of the phage T4 td gene
RT encodes a specific endonuclease.";
RL J. Biol. Chem. 264:10343-10346(1989).
CC -!- FUNCTION: This endonuclease is specific to the thymidylate synthase
CC (td) gene splice junction and is involved in intron homing.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SIMILARITY: To endonucleases of group I introns of fungi and phage.
CC {ECO:0000305}.
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DR EMBL; M12742; AAC12817.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42521.3; -; Genomic_DNA.
DR PIR; T10130; T10130.
DR RefSeq; NP_049849.3; NC_000866.4.
DR PDB; 1I3J; X-ray; 2.20 A; A=130-245.
DR PDB; 1LN0; X-ray; 2.00 A; A/B=1-97.
DR PDB; 1MK0; X-ray; 1.60 A; A=1-97.
DR PDB; 1T2T; X-ray; 2.50 A; A=130-245.
DR PDBsum; 1I3J; -.
DR PDBsum; 1LN0; -.
DR PDBsum; 1MK0; -.
DR PDBsum; 1T2T; -.
DR SMR; P13299; -.
DR DrugBank; DB04272; Citric acid.
DR MoonProt; P13299; -.
DR REBASE; 2625; I-TevI.
DR PRIDE; P13299; -.
DR GeneID; 1258722; -.
DR KEGG; vg:1258722; -.
DR EvolutionaryTrace; P13299; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0017053; C:transcription repressor complex; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:CAFA.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CAFA.
DR GO; GO:1990238; F:double-stranded DNA endodeoxyribonuclease activity; IDA:CACAO.
DR GO; GO:0004519; F:endonuclease activity; IDA:CAFA.
DR GO; GO:0043565; F:sequence-specific DNA binding; IMP:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CAFA.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:CAFA.
DR Gene3D; 3.40.1440.10; -; 1.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR006350; Intron_endoG1.
DR InterPro; IPR003611; NUMOD3.
DR Pfam; PF01541; GIY-YIG; 1.
DR SMART; SM00465; GIYc; 1.
DR SMART; SM00496; IENR2; 2.
DR SUPFAM; SSF82771; SSF82771; 1.
DR TIGRFAMs; TIGR01453; grpIintron_endo; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Intron homing; Magnesium; Nuclease;
KW Reference proteome.
FT CHAIN 1..245
FT /note="Intron-associated endonuclease 1"
FT /id="PRO_0000192792"
FT DOMAIN 1..88
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00977"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1MK0"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1MK0"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1MK0"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:1MK0"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:1MK0"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:1MK0"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1MK0"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:1MK0"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1MK0"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1T2T"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1I3J"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1I3J"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:1I3J"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1I3J"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1I3J"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1I3J"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:1I3J"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:1I3J"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1I3J"
SQ SEQUENCE 245 AA; 28232 MW; 29DF2ACF08ECD64C CRC64;
MKSGIYQIKN TLNNKVYVGS AKDFEKRWKR HFKDLEKGCH SSIKLQRSFN KHGNVFECSI
LEEIPYEKDL IIERENFWIK ELNSKINGYN IADATFGDTC STHPLKEEII KKRSETVKAK
MLKLGPDGRK ALYSKPGSKN GRWNPETHKF CKCGVRIQTS AYTCSKCRNR SGENNSFFNH
KHSDITKSKI SEKMKGKKPS NIKKISCDGV IFDCAADAAR HFKISSGLVT YRVKSDKWNW
FYINA
